Beta-amylase

Beta-amylase (EC 3.2.1.2; systematic name 4-α-D-glucan maltohydrolase) is an enzyme classified as an exohydrolase that catalyzes the hydrolysis of successive maltose units from the non-reducing ends of polysaccharides, such as starch and glycogen, by cleaving α-1,4 glycosidic bonds[1][2][3][4]. Beta-amylase is prolific in plants (notably seeds and fruit), bacteria, and fungi, but is not found in animal tissues except via microbial presence in the digestive tract[3]. The enzyme belongs to glycoside hydrolase family 14 (GH14), with different isoforms and oligomeric states existing in various species[1][2]. Its activity results in the release of beta-maltose and is key in processes like seed germination and fruit ripening, where starch is converted to maltose, creating a sweeter taste[3]. While beta-amylase is widely studied for its biochemical and industrial roles, it is not a typical drug target or known marker for therapeutic intervention in human diseases. The described enzymatic mechanism involves key residues acting as general acids and bases to facilitate cleavage of the glycosidic bond[1].

Other names

saccharogen amylaseglycogenasebeta-amylaseβ-amylase